scholarly journals The combination of electron capture dissociation and fixed charge derivatization increases sequence coverage for O-glycosylated and O-phosphorylated peptides

2007 ◽  
Vol 18 (8) ◽  
pp. 1405-1413 ◽  
Author(s):  
Julia Chamot-Rooke ◽  
Guillaume Rest ◽  
Alexandre Dalleu ◽  
Sylvie Bay ◽  
Jérôme Lemoine
Keyword(s):  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Fixed Charge ◽  
Sequence Coverage ◽  
Phosphorylated Peptides

Electron capture dissociation of singly and multiply phosphorylated peptides

2000 ◽  
Vol 14 (19) ◽  
pp. 1793-1800 ◽  
Author(s):  
Allan Stensballe ◽  
Ole N�rregaard Jensen ◽  
Jesper V. Olsen ◽  
Kim F. Haselmann ◽  
Roman A. Zubarev
Keyword(s):  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Phosphorylated Peptides

scholarly journals Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides

2010 ◽  
Vol 30 (6) ◽  
pp. 433-443 ◽  
Author(s):  
Karolina Kowalewska ◽  
Piotr Stefanowicz ◽  
Tomasz Ruman ◽  
Tomasz Frączyk ◽  
Wojciech Rode ◽  
...  
Keyword(s):  
Electron Capture ◽  
Electron Capture Dissociation ◽  
31P Nmr ◽  
Basic Amino Acid ◽  
Collision Induced Dissociation ◽  
Spectrometric Analysis ◽  
Phosphorylation Sites ◽  
Nmr Studies ◽  
Phosphorylated Peptides ◽  
Phosphorylation Reaction

Phosphorylation of proteins is an essential signalling mechanism in eukaryotic and prokaryotic cells. Although N-phosphorylation of basic amino acid is known for its importance in biological systems, it is still poorly explored in terms of products and mechanisms. In the present study, two MS fragmentation methods, ECD (electron-capture dissociation) and CID (collision-induced dissociation), were tested as tools for analysis of N-phosphorylation of three model peptides, RKRSRAE, RKRARKE and PLSRTLSVAAKK. The peptides were phosphorylated by reaction with monopotassium phosphoramidate. The results were confirmed by 1H NMR and 31P NMR studies. The ECD method was found useful for the localization of phosphorylation sites in unstable lysine-phosphorylated peptides. Its main advantage is a significant reduction of the neutral losses related to the phosphoramidate moiety. Moreover, the results indicate that the ECD–MS may be useful for analysis of regioselectivity of the N-phosphorylation reaction. Stabilities of the obtained lysine-phosphorylated peptides under various conditions were also tested.

scholarly journals Proteoform Differentiation using Tandem Trapped Ion Mobility, Electron Capture Dissociation, and ToF Mass Spectrometry

2021 ◽  
Author(s):  
Kevin Jeanne Dit Fouque ◽  
Desmond Kaplan ◽  
Valery G. Voinov ◽  
Frederik H. V. Holck ◽  
Ole N. Jensen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Ion Mobility ◽  
Trapped Ion

Negative-Ion Electron Capture Dissociation: Radical-Driven Fragmentation of Charge-Increased Gaseous Peptide Anions

2011 ◽  
Vol 133 (42) ◽  
pp. 16790-16793 ◽  
Author(s):  
Hyun Ju Yoo ◽  
Ning Wang ◽  
Shuyi Zhuang ◽  
Hangtian Song ◽  
Kristina Håkansson
Keyword(s):  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Negative Ion ◽  
Peptide Anions
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